Sodium in PDB 2wl5: Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A.

Enzymatic activity of Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A.

All present enzymatic activity of Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A.:
2.3.1.9;

Protein crystallography data

The structure of Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A., PDB code: 2wl5 was solved by G.Merilainen, V.Poikela, P.Kursula, R.K.Wierenga, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	19.39 / 1.80
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	84.700, 79.200, 153.000, 90.00, 92.50, 90.00
*R / R_free (%)*	22.1 / 25.7

Other elements in 2wl5:

The structure of Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A. also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A. (pdb code 2wl5). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A., PDB code: 2wl5:

Sodium binding site 1 out of 1 in 2wl5

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Sodium Binding Sites List in 2wl5

Sodium binding site 1 out of 1 in the Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A.

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Biosynthetic Thiolase From Z. Ramigera. Complex of the H348N Mutant with Coenzyme A. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Na1398 b:0.0 occ:1.00	CG2	B:ILE53	2.7	10.6	1.0
	CD1	B:LEU98	2.8	10.7	1.0
	CG	B:MET85	3.0	12.9	1.0
	CA	B:ALA95	3.1	7.1	1.0
	CB	B:LEU98	3.3	8.3	1.0
	CB	B:ALA95	3.4	9.0	1.0
	CH2	B:TRP83	3.5	6.1	1.0
	SD	B:MET85	3.6	9.7	1.0
	CG	B:LEU98	3.6	6.8	1.0
	CZ3	B:TRP83	3.7	7.2	1.0
	O	B:ALA95	3.8	6.3	1.0
	C	B:ALA95	4.0	9.4	1.0
	N	B:ALA95	4.0	2.1	1.0
	CB	B:ILE53	4.1	7.1	1.0
	CZ2	B:TRP83	4.1	9.6	1.0
	CB	B:MET85	4.2	6.0	1.0
	O	B:ARG94	4.3	7.0	1.0
	CE	B:MET85	4.4	7.1	1.0
	C	B:ARG94	4.5	12.4	1.0
	CE3	B:TRP83	4.6	7.3	1.0
	CD1	B:ILE53	4.6	11.5	1.0
	CA	B:LEU98	4.7	3.5	1.0
	CG1	B:ILE53	4.8	9.4	1.0
	CD2	B:LEU98	4.8	13.2	1.0
	CE2	B:TRP83	4.9	7.2	1.0

Reference:

G.Merilainen, V.Poikela, P.Kursula, R.K.Wierenga. The Thiolase Reaction Mechanism: the Importance of ASN316 and HIS348 For Stabilizing the Enolate Intermediate of the Claisen Condensation. Biochemistry V. 48 11011 2009.
ISSN: ISSN 0006-2960
PubMed: 19842716
DOI: 10.1021/BI901069H

Page generated: Mon Oct 7 04:42:29 2024

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